B6YRL9 (PYRDB_AZOPC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit
Short name=DHOD B
Short name=DHODase B
Short name=DHOdehase B
EC=1.3.1.14

Alternative name(s):
Dihydrdoorotate oxidase B
Orotate reductase (NADH)

Gene names

Name:	pyrD
Ordered Locus Names:	CFPG_578

Organism

Azobacteroides pseudotrichonymphae genomovar. CFP2 [Complete proteome] [HAMAP]

Taxonomic identifier

511995 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Candidatus Azobacteroides

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of dihydroorotate to orotate with NAD+ as electron acceptor By similarity. HAMAP MF_00224
Catalytic activity	(S)-dihydroorotate + NAD+ = orotate + NADH. HAMAP MF_00224
Cofactor	Binds 1 FMN per subunit By similarity. HAMAP MF_00224
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1. HAMAP MF_00224
Subunit structure	Heterotetramer of 2 PyrK and 2 PyrD type B subunits By similarity.
Subcellular location	Cytoplasm By similarity HAMAP MF_00224.
Sequence similarities	Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Cytoplasm
Ligand	FMN Flavoprotein NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro UMP biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dihydroorotate oxidase activity Inferred from electronic annotation. Source: InterPro orotate reductase (NADH) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 302	302	Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit HAMAP MF_00224		PRO_1000100215
Regions
	Nucleotide binding	45 – 46	2	FMN By similarity
	Nucleotide binding	243 – 244	2	FMN By similarity
	Nucleotide binding	265 – 266	2	FMN By similarity
	Region	69 – 73	5	Substrate binding By similarity
	Region	192 – 193	2	Substrate binding By similarity
Sites
	Active site	130	1	Nucleophile
	Binding site	21	1	FMN By similarity
	Binding site	45	1	Substrate By similarity
	Binding site	99	1	FMN By similarity
	Binding site	127	1	FMN By similarity
	Binding site	127	1	Substrate By similarity
	Binding site	165	1	FMN By similarity
	Binding site	191	1	FMN; via carbonyl oxygen By similarity
	Binding site	217	1	FMN; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	B6YRL9 [UniParc]. Last modified January 20, 2009. Version 1. Checksum: B5EEAFF50FA458B0	FASTA	302	32,512
	10 20 30 40 50 60 MADLNINIGK LKFKNPVLAA SGTFGYGIEY SDFVDLSKIG GIFTKGITLY HREGNDYPRM 70 80 90 100 110 120 AETSSGMLNA VGLQNRGVTY FIKNIYPKVK NIETNIMVNI SGSTIEDCVS CAEKINELDK 130 140 150 160 170 180 IPAIELNISC PNMKQGGMAF GTNCSNASEI VNAVRKVYHK ILIVKLSPNV TDITEIAKAV 190 200 210 220 230 240 EIAGADAVSL INTLIGMAID IKIKKPILST VTGGLSGPCI KPIALRMVYQ TYKIVKIPII 250 260 270 280 290 300 GLGGISNSDD AIEFILAGAS AIQVGTYNFI DPTISTKIVD GINAYLDKYH LLSIKELVGE LL

References

[1]

"Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT protist cells in termite gut." Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M. Science 322:1108-1109(2008) [PubMed: 19008447] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP010656 Genomic DNA. Translation: BAG83841.1.
RefSeq	YP_002309252.1. NC_011565.1.
3D structure databases
ProteinModelPortal	B6YRL9.
ModBase	Search...
Protein-protein interaction databases
STRING	B6YRL9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7039414.
GenomeReviews	Gene locus CFPG_578 in contig AP010656_GR.
KEGG	aps:CFPG_578.
PATRIC	31963062. VBICanAzo57536_0884.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG472415.
OMA	VALRMVW.
ProtClustDB	PRK07259.
Family and domain databases
HAMAP	MF_00224. DHO_dh_type1. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR005720. Dihydroorotate_DH. IPR024920. Dihydroorotate_DH_1. IPR012135. Dihydroorotate_DH_1_2. IPR001295. Dihydroorotate_DH_CS. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K00226.
Pfam	PF01180. DHO_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMs	TIGR01037. PyrD_sub1_fam. 1 hit.
PROSITE	PS00911. DHODEHASE_1. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRDB_AZOPC

Accession

Primary (citable) accession number: B6YRL9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	January 20, 2009
Last modified:	January 25, 2012
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program